Evidence map›Paper›PMID 34164097›Full record

ArticleChemical science2021

Snapshotting the transient conformations and tracing the multiple pathways of single peptide folding using a solid-state nanopore.

Shao-Chuang Liu, Yi-Lun Ying, Wei-Hua Li, Yong-Jing Wan, Yi-Tao Long

Abstract read
In one paragraph

Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

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  17. Single-Molecule Binding Assay Using Nanopores and Dimeric NP Conjugates.Advanced materials (Deerfield Beach, Fla.) · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Shao-Chuang LiuState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China ytlong@nju.edu.cn.ORCID https://orcid.org/0000-0002-1010-2321
Yi-Lun YingState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China ytlong@nju.edu.cn.ORCID https://orcid.org/0000-0001-6217-256X
Wei-Hua LiShanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology Shanghai 200237 P. R. China.ORCID https://orcid.org/0000-0001-7055-9836
Yong-Jing WanSchool of Information Science and Engineering, East China University of Science and Technology Shanghai 200237 P. R. China.ORCID https://orcid.org/0000-0002-3722-7271
Yi-Tao LongState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China ytlong@nju.edu.cn.ORCID https://orcid.org/0000-0003-2571-7457

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A fundamental question relating to protein folding/unfolding is the time evolution of the folding of a protein into its precisely defined native structure. The proper identification of transition conformations is essential for accurately describing the dynamic protein folding/unfolding pathways. Owing to the rapid transitions and sub-nm conformation differences involved, the acquisition of the transient conformations and dynamics of proteins is difficult due to limited instrumental resolution. Using the electrochemical confinement effect of a solid-state nanopore, we were able to snapshot the transient conformations and trace the multiple transition pathways of a single peptide inside a nanopore. By combining the results with a Markov chain model, this new single-molecule technique is applied to clarify the transition pathways of the β-hairpin peptide, which shows nonequilibrium fluctuations among several blockage current stages. This method enables the high-throughput investigation of transition pathways experimentally to access previously obscure peptide dynamics, which is significant for understanding the folding/unfolding mechanisms and misfolding of peptides or proteins.

Identifiers

PMID34164097
PMCPMC8179386

What Socratic holds

Textmetadata
LicenceCC BY-NC
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.